Zobrazeno 1 - 10
of 21
pro vyhledávání: '"J C Solheim"'
Publikováno v:
The Journal of Immunology. 158:2236-2241
Newly synthesized class I heavy (H) chain/beta 2m heterodimers awaiting peptides in the endoplasmic reticulum are associated with the transporter associated with Ag processing (TAP). We present evidence here that calreticulin, but not calnexin, displ
Publikováno v:
The Journal of Immunology. 155:4726-4733
To define the rules governing de novo assembly of the trimeric class I complex, we have identified the class I folding/assembly intermediates associated with calnexin or TAP, using both human and mouse cell lines. To better characterize the class I H
Publikováno v:
The Journal of Immunology. 154:1188-1197
To monitor conformational changes in MHC class I structure induced by interaction with peptide or beta 2-microglobulin (beta 2-m), we have taken a serologic approach. Previous studies by us and others have defined circumstances wherein specific pepti
Publikováno v:
The Journal of Immunology. 154:47-57
We have examined the ability of beta 2-m- mice to produce CD4-8+ T cells by generating CD8+ CTLs to a defined ligand. We report here the first demonstration of peptide-specific, self-class I MHC-restricted CTLs from beta 2-m-deficient mice. We have u
Autor:
J C Solheim, B M Carreno, J D Smith, J Gorka, N B Myers, Z Wen, J M Martinko, D R Lee, T H Hansen
Publikováno v:
The Journal of Immunology. 151:5387-5397
CTL recognize class I MHC/peptide complexes on the surface of target cells. Crystallographic and serologic data have indicated that peptide ligands can influence the conformation of class I molecules and hence T cell recognition. How the binding of p
Publikováno v:
The Journal of Immunology. 150:800-811
We have investigated the TCR gene usage in a panel of H-2Ld-restricted, tum- peptide-specific CTL clones. These clones possess identical MHC restriction and peptide specificity, yet they vary dramatically in the amount of peptide required to sensitiz
Publikováno v:
The Journal of Immunology. 158:541-543
Class I MHC heavy chains associate with many proteins in the endoplasmic reticulum, including TAP, calnexin, calreticulin, and the newly defined tapasin molecule. Recent studies have begun to resolve the nature of how these proteins interact with cla
Publikováno v:
Tissue antigens. 59(1)
Prior to binding to antigenic peptide, the major histocompatibility complex (MHC) heavy chain associates with an assembly complex of proteins that includes calreticulin, tapasin, and the transporter associated with antigen processing (TAP). Our data
Autor:
H R, Turnquist, J C, Solheim
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 156
Publikováno v:
European journal of immunology. 30(10)
To explore the nature of amino acid substitutions that influence association with TAP, we compared a site-directed mutant of HLA-B*0702 (Y116D) to unmutated HLA-B7 in regard to TAP interaction. We found that the mutant had stronger association with T